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Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene
Microbial degradation is the main process controlling the environmental dissipation of the nematicide oxamyl. Despite that, little is known regarding the microorganisms involved in its biotransformation. We report the isolation of four oxamyl-degrading bacterial strains from an agricultural soil exh...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850150/ https://www.ncbi.nlm.nih.gov/pubmed/27199945 http://dx.doi.org/10.3389/fmicb.2016.00616 |
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author | Rousidou, Konstantina Chanika, Eleni Georgiadou, Dafne Soueref, Eftychia Katsarou, Demetra Kolovos, Panagiotis Ntougias, Spyridon Tourna, Maria Tzortzakakis, Emmanuel A. Karpouzas, Dimitrios G. |
author_facet | Rousidou, Konstantina Chanika, Eleni Georgiadou, Dafne Soueref, Eftychia Katsarou, Demetra Kolovos, Panagiotis Ntougias, Spyridon Tourna, Maria Tzortzakakis, Emmanuel A. Karpouzas, Dimitrios G. |
author_sort | Rousidou, Konstantina |
collection | PubMed |
description | Microbial degradation is the main process controlling the environmental dissipation of the nematicide oxamyl. Despite that, little is known regarding the microorganisms involved in its biotransformation. We report the isolation of four oxamyl-degrading bacterial strains from an agricultural soil exhibiting enhanced biodegradation of oxamyl. Multilocus sequence analysis (MLSA) assigned the isolated bacteria to different subgroups of the genus Pseudomonas. The isolated bacteria hydrolyzed oxamyl to oxamyl oxime, which was not further transformed, and utilized methylamine as a C and N source. This was further supported by the detection of methylamine dehydrogenase in three of the four isolates. All oxamyl-degrading strains carried a gene highly homologous to a carbamate-hydrolase gene cehA previously identified in carbaryl- and carbofuran-degrading strains. Transcription analysis verified its direct involvement in the hydrolysis of oxamyl. Selected isolates exhibited relaxed degrading specificity and transformed all carbamates tested including the oximino carbamates aldicarb and methomyl (structurally related to oxamyl) and the aryl-methyl carbamates carbofuran and carbaryl which share with oxamyl only the carbamate moiety. |
format | Online Article Text |
id | pubmed-4850150 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-48501502016-05-19 Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene Rousidou, Konstantina Chanika, Eleni Georgiadou, Dafne Soueref, Eftychia Katsarou, Demetra Kolovos, Panagiotis Ntougias, Spyridon Tourna, Maria Tzortzakakis, Emmanuel A. Karpouzas, Dimitrios G. Front Microbiol Microbiology Microbial degradation is the main process controlling the environmental dissipation of the nematicide oxamyl. Despite that, little is known regarding the microorganisms involved in its biotransformation. We report the isolation of four oxamyl-degrading bacterial strains from an agricultural soil exhibiting enhanced biodegradation of oxamyl. Multilocus sequence analysis (MLSA) assigned the isolated bacteria to different subgroups of the genus Pseudomonas. The isolated bacteria hydrolyzed oxamyl to oxamyl oxime, which was not further transformed, and utilized methylamine as a C and N source. This was further supported by the detection of methylamine dehydrogenase in three of the four isolates. All oxamyl-degrading strains carried a gene highly homologous to a carbamate-hydrolase gene cehA previously identified in carbaryl- and carbofuran-degrading strains. Transcription analysis verified its direct involvement in the hydrolysis of oxamyl. Selected isolates exhibited relaxed degrading specificity and transformed all carbamates tested including the oximino carbamates aldicarb and methomyl (structurally related to oxamyl) and the aryl-methyl carbamates carbofuran and carbaryl which share with oxamyl only the carbamate moiety. Frontiers Media S.A. 2016-04-29 /pmc/articles/PMC4850150/ /pubmed/27199945 http://dx.doi.org/10.3389/fmicb.2016.00616 Text en Copyright © 2016 Rousidou, Chanika, Georgiadou, Soueref, Katsarou, Kolovos, Ntougias, Tourna, Tzortzakakis and Karpouzas. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Rousidou, Konstantina Chanika, Eleni Georgiadou, Dafne Soueref, Eftychia Katsarou, Demetra Kolovos, Panagiotis Ntougias, Spyridon Tourna, Maria Tzortzakakis, Emmanuel A. Karpouzas, Dimitrios G. Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title | Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title_full | Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title_fullStr | Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title_full_unstemmed | Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title_short | Isolation of Oxamyl-degrading Bacteria and Identification of cehA as a Novel Oxamyl Hydrolase Gene |
title_sort | isolation of oxamyl-degrading bacteria and identification of ceha as a novel oxamyl hydrolase gene |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850150/ https://www.ncbi.nlm.nih.gov/pubmed/27199945 http://dx.doi.org/10.3389/fmicb.2016.00616 |
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